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PDBsum entry 4nsc
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Calcium binding protein
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PDB id
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4nsc
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Contents |
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310 a.a.
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316 a.a.
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330 a.a.
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330 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural and mechanistic insights into micu1 regulation of mitochondrial calcium uptake.
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Authors
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L.Wang,
X.Yang,
S.Li,
Z.Wang,
Y.Liu,
J.Feng,
Y.Zhu,
Y.Shen.
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Ref.
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Embo J, 2014,
33,
594-604.
[DOI no: ]
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PubMed id
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Abstract
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Mitochondrial calcium uptake is a critical event in various cellular activities.
Two recently identified proteins, the mitochondrial Ca(2+) uniporter (MCU),
which is the pore-forming subunit of a Ca(2+) channel, and mitochondrial calcium
uptake 1 (MICU1), which is the regulator of MCU, are essential in this event.
However, the molecular mechanism by which MICU1 regulates MCU remains elusive.
In this study, we report the crystal structures of Ca(2+)-free and Ca(2+)-bound
human MICU1. Our studies reveal that Ca(2+)-free MICU1 forms a hexamer that
binds and inhibits MCU. Upon Ca(2+) binding, MICU1 undergoes large
conformational changes, resulting in the formation of multiple oligomers to
activate MCU. Furthermore, we demonstrate that the affinity of MICU1 for Ca(2+)
is approximately 15-20 μM. Collectively, our results provide valuable details
to decipher the molecular mechanism of MICU1 regulation of mitochondrial calcium
uptake.
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